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A Peptide Derived from Phosphoinositide 3-kinase Inhibits Endocytosis and Influenza Virus Infection

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Title: A Peptide Derived from Phosphoinositide 3-kinase Inhibits Endocytosis and Influenza Virus Infection
Authors: Fujioka, Yoichiro Browse this author →KAKEN DB
Satoh, Aya O. Browse this author
Horiuchi, Kosui Browse this author
Fujioka, Mari Browse this author
Tsutsumi, Kaori Browse this author →KAKEN DB
Sasaki, Junko Browse this author →KAKEN DB
Nepal, Prabha Browse this author
Kashiwagi, Sayaka Browse this author
Paudel, Sarad Browse this author →KAKEN DB
Nishide, Shinya Browse this author →KAKEN DB
Nanbo, Asuka Browse this author →KAKEN DB
Sasaki, Takehiko Browse this author →KAKEN DB
Ohba, Yusuke Browse this author →KAKEN DB
Keywords: signal transduction
endocytosis
endosome
imaging
influenza virus
Issue Date: 2019
Publisher: Japan Society for Cell Biology
Journal Title: Cell structure and function
Volume: 44
Issue: 1
Start Page: 61
End Page: 74
Publisher DOI: 10.1247/csf.19001
Abstract: Endocytosis mediates the internalization and ingestion of a variety of endogenous or exogenous substances, including virus particles, under the control of intracellular signaling pathways. We have previously reported that the complex formed between the small GTPase Ras and phosphoinositide 3-kinase (PI3K) translocates from the plasma membrane to endosomes, signaling from which thereby regulates clathrin-independent endocytosis, endosome maturation, influenza virus internalization, and infection. However, the molecular mechanism by which the Ras-PI3K complex is recruited to endosomes remains unclear. Here, we have identified the amino acid sequence responsible for endosomal localization of the Ras-PI3K complex. PI3K lacking this sequence failed to translocate to endosomes, and expression of the peptide comprising this PI3K-derived sequence inhibited clathrin-independent endocytosis, influenza virus internalization, and infection. Moreover, treatment of cells with this peptide in an arginine-rich, cell-penetrating form successfully suppressed influenza virus infection in vitro and ex vivo, making this peptide a potential therapeutic agent against influenza virus infection.
Rights: http://creativecommons.org/licenses/BY/4.0/
Type: article
URI: http://hdl.handle.net/2115/76512
Appears in Collections:医学院・医学研究院 (Graduate School of Medicine / Faculty of Medicine) > 雑誌発表論文等 (Peer-reviewed Journal Articles, etc)

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